ITIH1_BOVIN
ID ITIH1_BOVIN Reviewed; 906 AA.
AC Q0VCM5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H1;
DE Short=ITI heavy chain H1;
DE Short=ITI-HC1;
DE Short=Inter-alpha-inhibitor heavy chain 1;
DE Flags: Precursor;
GN Name=ITIH1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GLYCOSYLATION AT SER-643 AND THR-648, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA Darula Z., Medzihradszky K.F.;
RT "Affinity enrichment and characterization of mucin core-1 type
RT glycopeptides from bovine serum.";
RL Mol. Cell. Proteomics 8:2515-2526(2009).
CC -!- FUNCTION: May act as a carrier of hyaluronan in serum or as a binding
CC protein between hyaluronan and other matrix protein, including those on
CC cell surfaces in tissues to regulate the localization, synthesis and
CC degradation of hyaluronan which are essential to cells undergoing
CC biological processes. {ECO:0000250}.
CC -!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or
CC two heavy chains (HC) and one light chain, bikunin. Inter-alpha-
CC inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin.
CC Interacts with TNFAIP6 (via Link and CUB domains).
CC {ECO:0000250|UniProtKB:P19827}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate
CC esterified to the alpha-carboxyl of the C-terminal aspartate after
CC propeptide cleavage. {ECO:0000250}.
CC -!- PTM: The S-linked glycan is composed of two 6-carbon sugars, possibly
CC Glc or Gal. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC120096; AAI20097.1; -; mRNA.
DR RefSeq; NP_001068821.1; NM_001075353.2.
DR AlphaFoldDB; Q0VCM5; -.
DR SMR; Q0VCM5; -.
DR STRING; 9913.ENSBTAP00000010318; -.
DR GlyConnect; 708; 2 O-Linked glycans (2 sites).
DR iPTMnet; Q0VCM5; -.
DR PaxDb; Q0VCM5; -.
DR PeptideAtlas; Q0VCM5; -.
DR PRIDE; Q0VCM5; -.
DR Ensembl; ENSBTAT00000010318; ENSBTAP00000010318; ENSBTAG00000007843.
DR GeneID; 508356; -.
DR KEGG; bta:508356; -.
DR CTD; 3697; -.
DR VEuPathDB; HostDB:ENSBTAG00000007843; -.
DR VGNC; VGNC:30334; ITIH1.
DR eggNOG; ENOG502RXR2; Eukaryota.
DR GeneTree; ENSGT00940000162180; -.
DR InParanoid; Q0VCM5; -.
DR OMA; FNFLEAM; -.
DR OrthoDB; 955432at2759; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000007843; Expressed in liver and 39 other tissues.
DR ExpressionAtlas; Q0VCM5; baseline.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR010600; ITI_HC_C.
DR InterPro; IPR013694; VIT.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF06668; ITI_HC_C; 1.
DR Pfam; PF08487; VIT; 1.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00609; VIT; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS51468; VIT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Phosphoprotein; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..29
FT /evidence="ECO:0000250"
FT /id="PRO_0000285681"
FT CHAIN 30..667
FT /note="Inter-alpha-trypsin inhibitor heavy chain H1"
FT /id="PRO_0000285682"
FT PROPEP 668..906
FT /evidence="ECO:0000250"
FT /id="PRO_0000285683"
FT DOMAIN 32..161
FT /note="VIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT DOMAIN 287..470
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 667
FT /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT /evidence="ECO:0000250"
FT CARBOHYD 55
FT /note="S-linked (Hex...) cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 643
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT CARBOHYD 648
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:19674964"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 906 AA; 101237 MW; CAA22A87BA2D6AC1 CRC64;
MGLRGLLCVC LVSLLALQAV AAQGSPTRNP KGGKKRMAVD AAVDGVVIRS LKVNCKVTSR
FAHYIITSQV VNSADTAKEV SFNVEIPKTA FISDFAITAD ENAFTGDIKD KVTAWKQYRK
AAISGENAGL VRASGRTMEQ FSIHIIVGPR SKATFRLTYE EVLRRKLMQY DIVIKVKPQQ
LVQHFEIDVD IFEPQGIRKL DVEASFLPKE LAAQLIKKSF SGKKGHVLFR PTVSQQQTCP
TCSTTLLNGD FKVTYDVNRD DACDLLVANN YFAHFFAPQN LKKLNKNVVF VIDISSSMEG
QKLKQTKEAL HKILGDMRPG DYFDLVLFGS AVQSWKGSLV QASPANLEAA RNFVQQFSLA
GATNLNGGLL RGIEILNKAQ QSLPELSNHA SILIMLTDGE PTEGVMDRTQ ILKNVRDGIK
GRFPLYNLGF GHDVDLNFLE VMSLENNGRV QRIYEDHDAT QQLQGFYEQV ANPLLRDVEL
LYPREAVSDL TQHRHKQYYE GSEIMVAGRI ADHKLSSFKA DVRAHGEGQE FMTTCLVDKE
EMKKLLRERG HMLENHVERL WAYLTIQELL AKRMKLEGQE KANVSAKALQ MSLAYQFVTP
LTSMTVRGMT DQDGLEPIID KPLDDYLPLE MVGPRKTFML QASQPAPTHS SLDIKKLPDQ
VTGVDTDPHF LIHVPQKEDT LCFNINEEPG VVLSLVQDPD TGFSVNGQLI GNEAGSPGKH
EGTYFGRLGI ANPATDFQLE VTPQNITLNP GSGGPVFSWR DQAFLRQNEV LVTINRKRNL
VVSVEDGGTF EVVLHRVWRG SAVRQDFLGF YVLDSHRMSA RTHGLLGQFF HPFDYKVSNL
HPGSDPTKTD ATMVVKNRRL TVTRGLQKDY RKDPRHGAEV TCWFIHNNGD GLIDGIHTDY
IVPDIF
